位置:首页 > 蛋白库 > GATB_BACSU
GATB_BACSU
ID   GATB_BACSU              Reviewed;         476 AA.
AC   O30509; O31499; O50554;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B;
DE            Short=Asp/Glu-ADT subunit B;
DE            EC=6.3.5.-;
GN   Name=gatB; Synonyms=yerN; OrderedLocusNames=BSU06690;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=9342321; DOI=10.1073/pnas.94.22.11819;
RA   Curnow A.W., Hong K.-W., Yuan R., Kim S.-I., Martins O., Winkler W.,
RA   Henkin T.M., Soell D.;
RT   "Glu-tRNAGln amidotransferase: a novel heterotrimeric enzyme required for
RT   correct decoding of glutamine codons during translation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11819-11826(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hong K.-W., Martins O.M., Kim S.-I., Soell D.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or
CC       Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC       or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC       tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC       presence of glutamine and ATP through an activated phospho-Asp-
CC       tRNA(Asn) or phospho-Glu-tRNA(Gln).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC         + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U49788; AAB87634.1; -; Genomic_DNA.
DR   EMBL; AF008553; AAB83965.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12489.2; -; Genomic_DNA.
DR   PIR; T51583; T51583.
DR   RefSeq; NP_388551.2; NC_000964.3.
DR   AlphaFoldDB; O30509; -.
DR   SMR; O30509; -.
DR   IntAct; O30509; 1.
DR   MINT; O30509; -.
DR   STRING; 224308.BSU06690; -.
DR   jPOST; O30509; -.
DR   PaxDb; O30509; -.
DR   PRIDE; O30509; -.
DR   DNASU; 936057; -.
DR   EnsemblBacteria; CAB12489; CAB12489; BSU_06690.
DR   GeneID; 936057; -.
DR   KEGG; bsu:BSU06690; -.
DR   PATRIC; fig|224308.43.peg.706; -.
DR   eggNOG; COG0064; Bacteria.
DR   InParanoid; O30509; -.
DR   BioCyc; BSUB:BSU06690-MON; -.
DR   BioCyc; MetaCyc:MON-13956; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR   GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 1.
DR   HAMAP; MF_00121; GatB; 1.
DR   InterPro; IPR004413; Apn/Gln-ADT_bsu.
DR   InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR   InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00133; gatB; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..476
FT                   /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT                   subunit B"
FT                   /id="PRO_0000148762"
FT   CONFLICT        27..28
FT                   /note="TP -> PN (in Ref. 2; AAB87634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43
FT                   /note="G -> A (in Ref. 2; AAB87634)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240..241
FT                   /note="FF -> GV (in Ref. 3; CAB12489)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310..311
FT                   /note="FA -> LP (in Ref. 3; CAB12489)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  53553 MW;  095B056BF4B44676 CRC64;
     MNFETVIGLE VHVELKTKSK IFSSSPTPFG AEANTQTSVI DLGYPGVLPV LNKEAVEFAM
     KAAMALNCEI ATDTKFDRKN YFYPDNPKAY QISQFDKPIG ENGWIEIEVG GKTKRIGITR
     LHLEEDAGKL THTGDGYSLV DFNRQGTPLV EIVSEPDIRT PEEAYAYLEK LKSIIQYTGV
     SDCKMEEGSL RCDANISLRP IGQEEFGTKT ELKNLNSFAF VQKGLEHEEK RQEQVLLSGF
     FIQQETRRYD EATKKTILMR VKEGSDDYRY FPEPDLVELY IDDEWKERVK ASIPELPDER
     RKRYIEELGF AAYDAMVLTL TKEMADFFEE TVQKGAEAKQ ASNWLMGEVS AYLNAEQKEL
     ADVALTPEGL AGMIKLIEKG TISSKIAKKV FKELIEKGGD AEKIVKEKGL VQISDEGVLL
     KLVTEALDNN PQSIEDFKNG KDRAIGFLVG QIMKASKGQA NPPMVNKILL EEIKKR
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024